ID A0A843KH16_9EURY Unreviewed; 236 AA. AC A0A843KH16; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 14-DEC-2022, entry version 5. DE RecName: Full=Adenosylcobinamide-GDP ribazoletransferase {ECO:0000256|ARBA:ARBA00015850, ECO:0000256|HAMAP-Rule:MF_00719}; DE EC=2.7.8.26 {ECO:0000256|ARBA:ARBA00013200, ECO:0000256|HAMAP-Rule:MF_00719}; DE AltName: Full=Cobalamin synthase {ECO:0000256|ARBA:ARBA00032853, ECO:0000256|HAMAP-Rule:MF_00719}; DE AltName: Full=Cobalamin-5'-phosphate synthase {ECO:0000256|ARBA:ARBA00032605, ECO:0000256|HAMAP-Rule:MF_00719}; GN Name=cobS {ECO:0000256|HAMAP-Rule:MF_00719, GN ECO:0000313|EMBL:MBP7144392.1}; GN ORFNames=KBA44_04200 {ECO:0000313|EMBL:MBP7144392.1}; OS Methanoculleus sp. OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus. OX NCBI_TaxID=90427 {ECO:0000313|EMBL:MBP7144392.1, ECO:0000313|Proteomes:UP000672306}; RN [1] {ECO:0000313|EMBL:MBP7144392.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Go_SlDig_bin_367 {ECO:0000313|EMBL:MBP7144392.1}; RA Schneider D.; RT "Metagenome-Assembled Genomes of different Wastewater Treatment Stages in RT Germany."; RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Joins adenosylcobinamide-GDP and alpha-ribazole to generate CC adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin CC 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- CC phosphate. {ECO:0000256|ARBA:ARBA00025228, ECO:0000256|HAMAP- CC Rule:MF_00719}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = CC adenosylcob(III)alamin 5'-phosphate + GMP + H(+); CC Xref=Rhea:RHEA:23560, ChEBI:CHEBI:15378, ChEBI:CHEBI:57918, CC ChEBI:CHEBI:58115, ChEBI:CHEBI:60487, ChEBI:CHEBI:60493; EC=2.7.8.26; CC Evidence={ECO:0000256|ARBA:ARBA00001017, ECO:0000256|HAMAP- CC Rule:MF_00719}; CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosylcob(III)inamide-GDP + alpha-ribazole = CC adenosylcob(III)alamin + GMP + H(+); Xref=Rhea:RHEA:16049, CC ChEBI:CHEBI:10329, ChEBI:CHEBI:15378, ChEBI:CHEBI:18408, CC ChEBI:CHEBI:58115, ChEBI:CHEBI:60487; EC=2.7.8.26; CC Evidence={ECO:0000256|ARBA:ARBA00000357, ECO:0000256|HAMAP- CC Rule:MF_00719}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_00719}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7. CC {ECO:0000256|ARBA:ARBA00004663, ECO:0000256|HAMAP-Rule:MF_00719}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00719}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00719}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the CobS family. {ECO:0000256|ARBA:ARBA00010561, CC ECO:0000256|HAMAP-Rule:MF_00719}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBP7144392.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JAGOJX010000020; MBP7144392.1; -; Genomic_DNA. DR AlphaFoldDB; A0A843KH16; -. DR UniPathway; UPA00148; UER00238. DR Proteomes; UP000672306; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051073; F:adenosylcobinamide-GDP ribazoletransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008818; F:cobalamin 5'-phosphate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule. DR HAMAP; MF_00719; CobS; 1. DR InterPro; IPR003805; CobS. DR PANTHER; PTHR34148; ADENOSYLCOBINAMIDE-GDP RIBAZOLETRANSFERASE; 1. DR Pfam; PF02654; CobS; 1. DR TIGRFAMs; TIGR00317; cobS; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_00719}; KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP- KW Rule:MF_00719}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00719}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00719}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00719}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_00719}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_00719}. FT TRANSMEM 35..67 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00719" FT TRANSMEM 101..120 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00719" FT TRANSMEM 126..149 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00719" FT TRANSMEM 161..180 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00719" FT TRANSMEM 186..205 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00719" SQ SEQUENCE 236 AA; 24265 MW; A3335B1105D67D17 CRC64; MKSVLALLQF CTALPLGKPV EFEHFARRSY IYPLAGYVIG GIAAGVVAWI GSPAVGAAVA LAVVLVLSGC NHFDGLLDFG DGLMAHGSRE KRIAAMTDRT TGAGAVAAGI IVTLVAFAGL QDTAPLWAAI LTAEVSAKVA MSYLTTLGVP FREGIHSYLH GFARPWFVVP ATLLALPLFL LPVSPMKIAL ALVAAAGIAA ALLALSRHLF GGVNGDVVGA ANEITRAGVI LLLALL //